Light-Induced Structural Changes in a Photosynthetic Reaction Center Caught by Laue Diffraction
Journal article, 2010

Photosynthetic reaction centers convert the energy content of light into a transmembrane potential difference and so provide the major pathway for energy input into the biosphere. We applied time-resolved Laue diffraction to study light-induced conformational changes in the photosynthetic reaction center complex of Blastochloris viridis. The side chain of TyrL162, which lies adjacent to the special pair of bacteriochlorophyll molecules that are photooxidized in the primary light conversion event of photosynthesis, was observed to move 1.3 angstroms closer to the special pair after photoactivation. Free energy calculations suggest that this movement results from the deprotonation of this conserved tyrosine residue and provides a mechanism for stabilizing the primary charge separation reactions of photosynthesis.

TIME-RESOLVED CRYSTALLOGRAPHY

SPECIAL PAIR

RHODOPSEUDOMONAS-VIRIDIS

VIRIDIS REACTION CENTERS

PROTEIN

ELECTRON-TRANSFER

CYTOCHROME

SPECTROSCOPY

RHODOBACTER-SPHAEROIDES

TEMPERATURE

Author

Annemarie Wöhri

Chalmers, Chemical and Biological Engineering, Molecular Imaging

Gergely Katona

University of Gothenburg

Linda C Johansson

University of Gothenburg

Emelie Fritz

University of Gothenburg

Erik Malmerberg

University of Gothenburg

Magnus Andersson

Chalmers, Chemical and Biological Engineering, Molecular Imaging

J Vincent

Uppsala University

Mattias Eklund

Uppsala University

Marco Cammarata

European Synchrotron Radiation Facility (ESRF)

Michael Wulff

European Synchrotron Radiation Facility (ESRF)

Stanford University

J Davidsson

Uppsala University

G. Groenhof

Max Planck Society

Richard Neutze

University of Gothenburg

Science

0036-8075 (ISSN)

Vol. 328 5978 630-633

Subject Categories

Chemical Sciences

DOI

10.1126/science.1186159

More information

Latest update

6/20/2018